ID H9GM91_ANOCA Unreviewed; 1378 AA.
AC H9GM91;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN Name=INSRR {ECO:0000313|Ensembl:ENSACAP00000015124.4};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000015124.4, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000015124.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000015124.4};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000015124.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001171,
CC ECO:0000256|RuleBase:RU000312};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily.
CC {ECO:0000256|RuleBase:RU000312}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_008120257.1; XM_008122050.2.
DR RefSeq; XP_016853434.1; XM_016997945.1.
DR STRING; 28377.ENSACAP00000015124; -.
DR Ensembl; ENSACAT00000015430.4; ENSACAP00000015124.4; ENSACAG00000015162.4.
DR GeneID; 100556999; -.
DR KEGG; acs:100556999; -.
DR CTD; 3645; -.
DR eggNOG; KOG4258; Eukaryota.
DR GeneTree; ENSGT00940000160437; -.
DR HOGENOM; CLU_000288_166_0_1; -.
DR OrthoDB; 1614410at2759; -.
DR TreeFam; TF351636; -.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000015162; Expressed in ovary and 2 other cell types or tissues.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005899; C:insulin receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005009; F:insulin receptor activity; IBA:GO_Central.
DR GO; GO:0043560; F:insulin receptor substrate binding; IBA:GO_Central.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:InterPro.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd00063; FN3; 3.
DR CDD; cd00064; FU; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000494; Rcpt_L-dom.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016246; Tyr_kinase_insulin-like_rcpt.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416:SF338; INSULIN RECEPTOR-RELATED PROTEIN; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 2.
DR PIRSF; PIRSF000620; Insulin_receptor; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00261; FU; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000620-
KW 2}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000620-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW ECO:0000256|RuleBase:RU000312};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000312};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000312};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1378
FT /note="Tyrosine-protein kinase receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032937941"
FT TRANSMEM 969..994
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 508..628
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 632..731
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 865..960
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1035..1316
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 761..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1171
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-1"
FT BINDING 1045
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT BINDING 1069
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1116..1122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT BINDING 1175..1176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT BINDING 1189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
SQ SEQUENCE 1378 AA; 155265 MW; 2E90E30AF4912F6A CRC64;
MGWKRGSFPP ASWEALLLFL SIFSMGPQPV TPEVCDSLDI RVDVSQLRRL ENCTIIEGNL
QILLMFTSSS EDFQPLSFPR LVMITEYLLL FRVYGLESLR DLFPNLAVIR GTSLFFNYAL
VIFEMPHLRD IGLFSLTNIL NGSVRIERNQ ELCHISTIDW SLLQPLHSLE HNIILHNKPV
EECADVCPGM LGVEKPCVQT QKGLTGQMEY RCWTSHNCQK VCPCKVGGRG GGAVEATDTA
AAACTGNGEC CNPECLGGCS RARDHRACVA CRHFELNGRC LRSCPELTYQ YEGWRCVTAE
HCASLHKVSE NPRDSSRFVI HQGQCLSECP SGYKRNDSSI FCHKCEGLCP KECKVGTKTI
DSTRAARDLT GCTLVEGNLI INIRRADNLI SDLQGSLGLI ETITGFLKIK HSFALISLSF
FKNLRLIRGD SMVDGNYTLY VLDNQNLQQL WDWSRHTLFI PAGKMYFAFN PRLCLSEIYR
MEEITGTKGR QNKAEINPRT NGDRASCKTQ TLRFVSNATE SDRIVLKWER YQPPEYRDLL
SFIVYYKESP FQNVTEYIGQ DACGANSWNV VDVDLPLNND QEPGVILQNL KPWTQYAIFV
RAITLTTAEE GRDYGAQSKV VYIRTMPAVP TVPRDVISMS NSSSHLIVRW KPPTQPNGNL
TYYLVLWQQL AEDSELFVND YCHKGLRLPT SSADTRFDMD NEGREDAEDE QCCPCQSPVG
QAQLGGETVS FQKKFENFLH NSIIIPRPPW KVTSINKVSH RIPKRRRDAA SAPAAGHLFA
DPSPPEVSRK TAAPNGTETD PMAQKDFRIS EDKVVRERTA IASLRHFTEY RIDIHACNHA
AQTVGCSAAT FVFARTMPEP QADNIPGNMT WEPAGKNTVL LRWKEPQNPN GLVLKYEIKY
SRESEKVVSV VCVSRHRYAQ YGGYHLALLQ PGNYSAKVRA TSLSGNGSWT GLIKFYILGP
VEEEEAGNVY VLLILMPVVL MVGIACLAIF VFLYNKKRST EGYPSGTLYA SVNPEYFSTS
NMYIPDEWEV PREKITVLRE LGQGSFGMVY EGIARDIEGE GQETRVALKT VNELATMRER
IEFLKEASVM KAFRCHHVVR LLGVVSQGQP ALVIMELMMR GDLKSFLRSL RPEAENNPGL
PPPSLKEMIQ MAGEIADGMA YLNAKKFVHR DLAARNCMVS EDFTVKIGDF GMTRDIYETD
YYRKSGKGLL PVRWMSPEAL KDGLFNTHSD IWSFGVVLWE IATLAEQPYQ GMSNEQVLHF
VMDNGILEKP ENCPEKLHEL MTWCWQQNPR LRPSFIQILE SIKEDMSSSF RTHSFFYSLE
NKHCSSWEVL DAETDQLLVS DASVLDVPNG RPLLSLGPYM EQGPPTECKP QPNGKPSL
//
